5c6g

Structural Insights into the Scc2-Scc4 Cohesin Loader

spinqualitylabelsall models 5c6g, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c6g is a 4 chain structure with sequence from Eremothecium gossypii ATCC 10895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q74ZR5_ASHGO Publication Abstract from PubMed The remarkable accuracy of eukaryotic cell division is partly maintained by the cohesin complex acting as a molecular glue to prevent premature sister chromatid separation. The loading of cohesin onto chromosomes is catalyzed by the Scc2-Scc4 loader complex. Here, we report the crystal structure of Scc4 bound to the N terminus of Scc2 and show that Scc4 is a tetratricopeptide repeat (TPR) superhelix. The Scc2 N terminus adopts an extended conformation and is entrapped by the core of the Scc4 superhelix. Electron microscopy (EM) analysis reveals that the Scc2-Scc4 loader complex comprises three domains: a head, body, and hook. Deletion studies unambiguously assign the Scc2N-Scc4 as the globular head domain, whereas in vitro cohesin loading assays show that the central body and the hook domains are sufficient to catalyze cohesin loading onto circular DNA, but not chromatinized DNA in vivo, suggesting a possible role for Scc4 as a chromatin adaptor. Structural Studies Reveal the Functional Modularity of the Scc2-Scc4 Cohesin Loader.,Chao WC, Murayama Y, Munoz S, Costa A, Uhlmann F, Singleton MR Cell Rep. 2015 Jul 22. pii: S2211-1247(15)00709-3. doi:, 10.1016/j.celrep.2015.06.071. PMID:26212329 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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